메뉴 건너뛰기




Volumn 123, Issue 3, 2010, Pages 392-400

Three-dimensional organization of promyelocytic leukemia nuclear bodies

Author keywords

4Pi microscopy; Promyelocytic leukemia nuclear bodies; Sumoylation

Indexed keywords

HETEROCHROMATIN PROTEIN 1; NUCLEAR PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN SP100; SUMO PROTEIN; UNCLASSIFIED DRUG;

EID: 76649083577     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.053496     Document Type: Article
Times cited : (95)

References (67)
  • 1
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • Bernardi, R. and Pandolfi, P. P. (2007). Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat. Rev. Mol. Cell. Biol. 8, 1006-1016.
    • (2007) Nat. Rev. Mol. Cell. Biol , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 2
    • 33845340785 scopus 로고    scopus 로고
    • H2AX chromatin structures and their response to DNA damage revealed by 4Pi microscopy
    • Bewersdorf, J., Bennett, B. and Knight, K. (2006). H2AX chromatin structures and their response to DNA damage revealed by 4Pi microscopy. Proc. Natl. Acad. Sci. USA 103, 18137-18142.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 18137-18142
    • Bewersdorf, J.1    Bennett, B.2    Knight, K.3
  • 3
    • 0034707690 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA
    • Boisvert, F. M., Hendzel, M. J. and Bazett-Jones, D. P. (2000a). Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J. Cell Biol. 148, 283-292.
    • (2000) J. Cell Biol , vol.148 , pp. 283-292
    • Boisvert, F.M.1    Hendzel, M.J.2    Bazett-Jones, D.P.3
  • 4
    • 0034707690 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA
    • Boisvert, F. M., Hendzel, M. J. and Bazett-Jones, D. P. (2000b). Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J. Cell Biol. 148, 283-292.
    • (2000) J. Cell Biol , vol.148 , pp. 283-292
    • Boisvert, F.M.1    Hendzel, M.J.2    Bazett-Jones, D.P.3
  • 5
    • 0036318221 scopus 로고    scopus 로고
    • Pondering the promyelocytic leukemia protein (PML) puzzle: Possible functions for PML nuclear bodies
    • Borden, K. L. (2002). Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies. Mol. Cell. Biol. 22, 5259-5269.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 5259-5269
    • Borden, K.L.1
  • 6
    • 53249134730 scopus 로고    scopus 로고
    • Pondering the puzzle of PML (promyelocytic leukemia) nuclear bodies: Can we fit the pieces together using an RNA regulon?
    • Borden, K. L. (2008). Pondering the puzzle of PML (promyelocytic leukemia) nuclear bodies: can we fit the pieces together using an RNA regulon? Biochim. Biophys. Acta 1783, 2145-2154.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2145-2154
    • Borden, K.L.1
  • 7
    • 0029918562 scopus 로고    scopus 로고
    • In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML
    • Borden, K. L., Lally, J. M., Martin, S. R., O'Reilly, N. J., Solomon, E. and Freemont, P. S. (1996). In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML. Proc. Natl. Acad. Sci. USA 93, 1601-1606.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1601-1606
    • Borden, K.L.1    Lally, J.M.2    Martin, S.R.3    O'Reilly, N.J.4    Solomon, E.5    Freemont, P.S.6
  • 8
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: Dynamic sensors of DNA damage and cellular stress
    • Dellaire, G. and Bazett-Jones, D. P. (2004). PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. BioEssays 26, 963-977.
    • (2004) BioEssays , vol.26 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 9
    • 0037133634 scopus 로고    scopus 로고
    • Fast 100-nm resolution 3D-microscope reveals structural plasticity of mitochondria in live yeast
    • Egner, A., Jakobs, S. and Hell, S. W. (2002). Fast 100-nm resolution 3D-microscope reveals structural plasticity of mitochondria in live yeast. Proc. Natl. Acad. Sci. USA 99, 3370-3375.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3370-3375
    • Egner, A.1    Jakobs, S.2    Hell, S.W.3
  • 10
    • 16244422998 scopus 로고    scopus 로고
    • ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection
    • Everett, R. D. and Murray, J. (2005). ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection. J. Virol. 79, 5078-5089.
    • (2005) J. Virol , vol.79 , pp. 5078-5089
    • Everett, R.D.1    Murray, J.2
  • 11
    • 0033380850 scopus 로고    scopus 로고
    • Cell cycle regulation of PML modification and ND10 composition
    • Everett, R. D., Lomonte, P., Sternsdorf, T., van Driel, R. and Orr, A. (1999). Cell cycle regulation of PML modification and ND10 composition. J. Cell Sci. 112, 4581-4588.
    • (1999) J. Cell Sci , vol.112 , pp. 4581-4588
    • Everett, R.D.1    Lomonte, P.2    Sternsdorf, T.3    van Driel, R.4    Orr, A.5
  • 12
    • 33746827706 scopus 로고    scopus 로고
    • PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0
    • Everett, R. D., Rechter, S., Papior, P., Tavalai, N., Stamminger, T. and Orr, A. (2006). PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0. J. Virol. 80, 7995-8005.
    • (2006) J. Virol , vol.80 , pp. 7995-8005
    • Everett, R.D.1    Rechter, S.2    Papior, P.3    Tavalai, N.4    Stamminger, T.5    Orr, A.6
  • 13
    • 0036903851 scopus 로고    scopus 로고
    • Nanosizing of fluorescent objects by spatially modulated illumination microscopy
    • Failla, A. V., Spoeri, U., Albrecht, B., Kroll, A. and Cremer, C. (2002). Nanosizing of fluorescent objects by spatially modulated illumination microscopy. Appl. Optics 41, 7275-7283.
    • (2002) Appl. Optics , vol.41 , pp. 7275-7283
    • Failla, A.V.1    Spoeri, U.2    Albrecht, B.3    Kroll, A.4    Cremer, C.5
  • 14
    • 24644522876 scopus 로고    scopus 로고
    • Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3
    • Fu, C., Ahmed, K., Ding, H., Ding, X., Lan, J., Yang, Z., Miao, Y., Zhu, Y., Shi, Y., Zhu, J. et al. (2005). Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3. Oncogene 24, 5401-5413.
    • (2005) Oncogene , vol.24 , pp. 5401-5413
    • Fu, C.1    Ahmed, K.2    Ding, H.3    Ding, X.4    Lan, J.5    Yang, Z.6    Miao, Y.7    Zhu, Y.8    Shi, Y.9    Zhu, J.10
  • 15
    • 0026326963 scopus 로고
    • Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia
    • Goddard, A. D., Borrow, J., Freemont, P. S. and Solomon, E. (1991). Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia. Science 254, 1371-1374.
    • (1991) Science , vol.254 , pp. 1371-1374
    • Goddard, A.D.1    Borrow, J.2    Freemont, P.S.3    Solomon, E.4
  • 18
    • 10044248656 scopus 로고    scopus 로고
    • Cooperative 4Pi excitation and detection yields 7-fold sharper optical sections in live cell microscopy
    • Gugel, H., Bewersdorf, J., Jakobs, S., Engelhardt, J., Storz, R. and Hell, S. W. (2004). Cooperative 4Pi excitation and detection yields 7-fold sharper optical sections in live cell microscopy. Biophys. J. 87, 4146-4152.
    • (2004) Biophys. J , vol.87 , pp. 4146-4152
    • Gugel, H.1    Bewersdorf, J.2    Jakobs, S.3    Engelhardt, J.4    Storz, R.5    Hell, S.W.6
  • 19
    • 34249945258 scopus 로고    scopus 로고
    • Far-field optical nanoscopy
    • Hell, S. W. (2007). Far-field optical nanoscopy. Science 316, 1153-1158.
    • (2007) Science , vol.316 , pp. 1153-1158
    • Hell, S.W.1
  • 20
    • 84975659980 scopus 로고
    • Properties of a 4Pi-confocal fluorescence microscope
    • Hell, S. and Stelzer, E. H. K. (1992). Properties of a 4Pi-confocal fluorescence microscope. J. Opt. Soc. Am. A. 9, 2159-2166.
    • (1992) J. Opt. Soc. Am. A , vol.9 , pp. 2159-2166
    • Hell, S.1    Stelzer, E.H.K.2
  • 21
    • 47749125333 scopus 로고    scopus 로고
    • 4Pi microscopy of the nuclear pore complex
    • Hüve, J., Wesselmann, R., Kahms, M. and Peters, R. (2008). 4Pi microscopy of the nuclear pore complex. Biophys. J. 95, 877-885.
    • (2008) Biophys. J , vol.95 , pp. 877-885
    • Hüve, J.1    Wesselmann, R.2    Kahms, M.3    Peters, R.4
  • 22
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1
    • Ishov, A. M., Sotnikov, A. G., Negorev, D., Vladimirova, O. V., Neff, N., Kamitani, T., Yeh, E. T., Strauss, J. F., 3rd and Maul, G. G. (1999). PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1. J. Cell Biol. 147, 221-234.
    • (1999) J. Cell Biol , vol.147 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3    Vladimirova, O.V.4    Neff, N.5    Kamitani, T.6    Yeh, E.T.7    Strauss 3rd, J.F.8    Maul, G.G.9
  • 25
    • 15644368249 scopus 로고    scopus 로고
    • Covalent modification of PML by the sentrin family of ubiquitin-like proteins
    • Kamitani, T., Nguyen, H. P., Kito, K., Fukuda-Kamitani, T. and Yeh, E. T. (1998b). Covalent modification of PML by the sentrin family of ubiquitin-like proteins. J. Biol. Chem. 273, 3117-3120.
    • (1998) J. Biol. Chem , vol.273 , pp. 3117-3120
    • Kamitani, T.1    Nguyen, H.P.2    Kito, K.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 26
    • 0026583943 scopus 로고
    • Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): Structural similarities with a new family of oncoproteins
    • Kastner, P., Perez, A., Lutz, Y., Rochette-Egly, C., Gaub, M. P., Durand, B., Lanotte, M., Berger, R. and Chambon, P. (1992). Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins. EMBO J. 11, 629-642.
    • (1992) EMBO J , vol.11 , pp. 629-642
    • Kastner, P.1    Perez, A.2    Lutz, Y.3    Rochette-Egly, C.4    Gaub, M.P.5    Durand, B.6    Lanotte, M.7    Berger, R.8    Chambon, P.9
  • 29
    • 27744466964 scopus 로고    scopus 로고
    • Synthetic, self-assembly ABCD nanoparticles; a structural paradigm for viable synthetic non-viral vectors
    • Kostarelos, K. and Miller, A. D. (2005). Synthetic, self-assembly ABCD nanoparticles; a structural paradigm for viable synthetic non-viral vectors. Chem. Soc. Rev. 34, 970-994.
    • (2005) Chem. Soc. Rev , vol.34 , pp. 970-994
    • Kostarelos, K.1    Miller, A.D.2
  • 30
    • 0035908032 scopus 로고    scopus 로고
    • Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation
    • Lallemand-Breitenbach, V., Zhu, J., Puvion, F., Koken, M., Honore, N., Doubeikovsky, A., Duprez, E., Pandolfi, P. P., Puvion, E., Freemont, P. et al. (2001). Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation. J. Exp. Med. 193, 1361-1371.
    • (2001) J. Exp. Med , vol.193 , pp. 1361-1371
    • Lallemand-Breitenbach, V.1    Zhu, J.2    Puvion, F.3    Koken, M.4    Honore, N.5    Doubeikovsky, A.6    Duprez, E.7    Pandolfi, P.P.8    Puvion, E.9    Freemont, P.10
  • 32
    • 33847349839 scopus 로고    scopus 로고
    • 4Pi microscopy with linear fluorescence excitation
    • Lang, M., Engelhardt, J. and Hell, S. W. (2007a). 4Pi microscopy with linear fluorescence excitation. Opt. Lett. 32, 259-261.
    • (2007) Opt. Lett , vol.32 , pp. 259-261
    • Lang, M.1    Engelhardt, J.2    Hell, S.W.3
  • 33
    • 33847752217 scopus 로고    scopus 로고
    • 4Pi microscopy of type A with 1-photon excitation in biological fluorescence imaging
    • Lang, M., Müller, T., Engelhardt, J. and Hell, S. W. (2007b). 4Pi microscopy of type A with 1-photon excitation in biological fluorescence imaging. Opt. Express 15, 2459-2467.
    • (2007) Opt. Express , vol.15 , pp. 2459-2467
    • Lang, M.1    Müller, T.2    Engelhardt, J.3    Hell, S.W.4
  • 34
    • 0030027449 scopus 로고    scopus 로고
    • Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene, PML
    • Le, X. F., Yang, P. and Chang, K. S. (1996). Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene, PML. J. Biol. Chem. 271, 130-135.
    • (1996) J. Biol. Chem , vol.271 , pp. 130-135
    • Le, X.F.1    Yang, P.2    Chang, K.S.3
  • 35
    • 33750491062 scopus 로고    scopus 로고
    • Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors
    • Lin, D. Y., Huang, Y. S., Jeng, J. C., Kuo, H. Y., Chang, C. C., Chao, T. T., Ho, C. C., Chen, Y. C., Lin, T. P., Fang, H. I. et al. (2006). Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol. Cell 24, 341-354.
    • (2006) Mol. Cell , vol.24 , pp. 341-354
    • Lin, D.Y.1    Huang, Y.S.2    Jeng, J.C.3    Kuo, H.Y.4    Chang, C.C.5    Chao, T.T.6    Ho, C.C.7    Chen, Y.C.8    Lin, T.P.9    Fang, H.I.10
  • 36
    • 0041856232 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation
    • Louria-Hayon, I., Grossman, T., Sionov, R. V., Alsheich, O., Pandolfi, P. P. and Haupt, Y. (2003). The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation. J. Biol. Chem. 278, 33134-33141.
    • (2003) J. Biol. Chem , vol.278 , pp. 33134-33141
    • Louria-Hayon, I.1    Grossman, T.2    Sionov, R.V.3    Alsheich, O.4    Pandolfi, P.P.5    Haupt, Y.6
  • 38
    • 39049093685 scopus 로고    scopus 로고
    • In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy
    • Matic, I., van Hagen, M., Schimmel, J., Macek, B., Ogg, S. C., Tatham, M. H., Hay, R. T., Lamond, A. I., Mann, M. and Vertegaal, A. C. (2008). In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy. Mol. Cell Proteomics 7, 132-144.
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 132-144
    • Matic, I.1    van Hagen, M.2    Schimmel, J.3    Macek, B.4    Ogg, S.C.5    Tatham, M.H.6    Hay, R.T.7    Lamond, A.I.8    Mann, M.9    Vertegaal, A.C.10
  • 39
    • 0033561797 scopus 로고    scopus 로고
    • Deconstructing a disease: RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia
    • Melnick, A. and Licht, J. D. (1999). Deconstructing a disease: RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia. Blood 93, 3167-3215.
    • (1999) Blood , vol.93 , pp. 3167-3215
    • Melnick, A.1    Licht, J.D.2
  • 40
  • 42
    • 0002977820 scopus 로고    scopus 로고
    • Coherent use of opposing lenses for axial resolution increase in fluorescence microscopy. II. Power and limitation of nonlinear image restoration
    • Nagorni, M. and Hell, S. W. (2001). Coherent use of opposing lenses for axial resolution increase in fluorescence microscopy. II. Power and limitation of nonlinear image restoration. J. Opt. Soc. Am. A 18, 49-54.
    • (2001) J. Opt. Soc. Am. A , vol.18 , pp. 49-54
    • Nagorni, M.1    Hell, S.W.2
  • 43
    • 33746470038 scopus 로고    scopus 로고
    • Telomerase-independent maintenance of mammalian telomeres
    • eds T. de Lange, V. Lundblad and E. Blackburn, pp, Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Neumann, A. A. and Reddel, R. R. (2006). Telomerase-independent maintenance of mammalian telomeres. In Telomeres (eds T. de Lange, V. Lundblad and E. Blackburn), pp. 163-198. Cold Spring Harbor: Cold Spring Harbor Laboratory Press.
    • (2006) Telomeres , pp. 163-198
    • Neumann, A.A.1    Reddel, R.R.2
  • 45
    • 0027328057 scopus 로고
    • PMLRAR homodimers: Distinct DNA binding properties and heteromeric interactions with RXR
    • Perez, A., Kastner, P., Sethi, S., Lutz, Y., Reibel, C. and Chambon, P. (1993). PMLRAR homodimers: distinct DNA binding properties and heteromeric interactions with RXR. EMBO J. 12, 3171-3182.
    • (1993) EMBO J , vol.12 , pp. 3171-3182
    • Perez, A.1    Kastner, P.2    Sethi, S.3    Lutz, Y.4    Reibel, C.5    Chambon, P.6
  • 46
    • 34447129654 scopus 로고    scopus 로고
    • The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins
    • Potts, P. R. and Yu, H. (2007). The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins. Nat. Struct. Mol. Biol. 14, 581-590.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 581-590
    • Potts, P.R.1    Yu, H.2
  • 47
    • 33646859205 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein stimulates SUMO conjugation in yeast
    • Quimby, B. B., Yong-Gonzalez, V., Anan, T., Strunnikov, A. V. and Dasso, M. (2006). The promyelocytic leukemia protein stimulates SUMO conjugation in yeast. Oncogene 25, 2999-3005.
    • (2006) Oncogene , vol.25 , pp. 2999-3005
    • Quimby, B.B.1    Yong-Gonzalez, V.2    Anan, T.3    Strunnikov, A.V.4    Dasso, M.5
  • 48
    • 0001106323 scopus 로고
    • Electromagnetic diffraction in optical systems II. Structure of the image field in an aplanatic system
    • Richards, B. and Wolf, E. (1959). Electromagnetic diffraction in optical systems II. Structure of the image field in an aplanatic system. Proc. R. Soc. Lond. A 253, 358-379.
    • (1959) Proc. R. Soc. Lond. A , vol.253 , pp. 358-379
    • Richards, B.1    Wolf, E.2
  • 49
    • 9644266570 scopus 로고    scopus 로고
    • Characterization of a nuclear compartment shared by nuclear bodies applying ectopic protein expression and correlative light and electron microscopy
    • Richter, K., Reichenzeller, M., Gorisch, S. M., Schmidt, U., Scheuermann, M. O., Herrmann, H. and Lichter, P. (2005). Characterization of a nuclear compartment shared by nuclear bodies applying ectopic protein expression and correlative light and electron microscopy. Exp. Cell Res. 303, 128-137.
    • (2005) Exp. Cell Res , vol.303 , pp. 128-137
    • Richter, K.1    Reichenzeller, M.2    Gorisch, S.M.3    Schmidt, U.4    Scheuermann, M.O.5    Herrmann, H.6    Lichter, P.7
  • 50
    • 33646031179 scopus 로고    scopus 로고
    • In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies
    • Saitoh, N., Uchimura, Y., Tachibana, T., Sugahara, S., Saitoh, H. and Nakao, M. (2006). In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies. Exp. Cell Res. 312, 1418-1430.
    • (2006) Exp. Cell Res , vol.312 , pp. 1418-1430
    • Saitoh, N.1    Uchimura, Y.2    Tachibana, T.3    Sugahara, S.4    Saitoh, H.5    Nakao, M.6
  • 51
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • Salomoni, P. and Pandolfi, P. P. (2002). The role of PML in tumor suppression. Cell 108, 165-170.
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 52
    • 44849143636 scopus 로고    scopus 로고
    • New insights into the role of PML in tumour suppression
    • Salomoni, P., Ferguson, B. J., Wyllie, A. H. and Rich, T. (2008). New insights into the role of PML in tumour suppression. Cell Res. 18, 622-640.
    • (2008) Cell Res , vol.18 , pp. 622-640
    • Salomoni, P.1    Ferguson, B.J.2    Wyllie, A.H.3    Rich, T.4
  • 54
    • 0035028618 scopus 로고    scopus 로고
    • Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: Role of SUMO modification
    • Seeler, J. S., Marchio, A., Losson, R., Desterro, J. M., Hay, R. T., Chambon, P. and Dejean, A. (2001). Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modification. Mol. Cell. Biol. 21, 3314-3324.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 3314-3324
    • Seeler, J.S.1    Marchio, A.2    Losson, R.3    Desterro, J.M.4    Hay, R.T.5    Chambon, P.6    Dejean, A.7
  • 57
    • 33846108375 scopus 로고    scopus 로고
    • 2,2′-Thiodiethanol: A new water soluble mounting medium for high resolution optical microscopy
    • Staudt, T., Lang, M., Medda, R., Engelhardt, J. and Hell, S. W. (2007). 2,2′-Thiodiethanol: a new water soluble mounting medium for high resolution optical microscopy. Microsc. Res. Tech. 70, 1-9.
    • (2007) Microsc. Res. Tech , vol.70 , pp. 1-9
    • Staudt, T.1    Lang, M.2    Medda, R.3    Engelhardt, J.4    Hell, S.W.5
  • 58
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1
    • Sternsdorf, T., Jensen, K. and Will, H. (1997). Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J. Cell Biol. 139, 1621-1634.
    • (1997) J. Cell Biol , vol.139 , pp. 1621-1634
    • Sternsdorf, T.1    Jensen, K.2    Will, H.3
  • 59
    • 0033617169 scopus 로고    scopus 로고
    • The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers
    • Sternsdorf, T., Jensen, K., Reich, B. and Will, H. (1999). The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J. Biol. Chem. 274, 12555-12566.
    • (1999) J. Biol. Chem , vol.274 , pp. 12555-12566
    • Sternsdorf, T.1    Jensen, K.2    Reich, B.3    Will, H.4
  • 62
    • 33747373841 scopus 로고    scopus 로고
    • Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation
    • Uchimura, Y., Ichimura, T., Uwada, J., Tachibana, T., Sugahara, S., Nakao, M. and Saitoh, H. (2006). Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation. J. Biol. Chem. 281, 23180-23190.
    • (2006) J. Biol. Chem , vol.281 , pp. 23180-23190
    • Uchimura, Y.1    Ichimura, T.2    Uwada, J.3    Tachibana, T.4    Sugahara, S.5    Nakao, M.6    Saitoh, H.7
  • 64
    • 41549115723 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy to assess the mobility of nuclear proteins
    • Weidtkamp-Peters, S., Weisshart, K., Schmiedeberg, L. and Hemmerich, P. (2009). Fluorescence correlation spectroscopy to assess the mobility of nuclear proteins. Methods Mol. Biol. 464, 321-341.
    • (2009) Methods Mol. Biol , vol.464 , pp. 321-341
    • Weidtkamp-Peters, S.1    Weisshart, K.2    Schmiedeberg, L.3    Hemmerich, P.4
  • 65
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells
    • Weis, K., Rambaud, S., Lavau, C., Jansen, J., Carvalho, T., Carmo-Fonseca, M., Lamond, A. and Dejean, A. (1994). Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells. Cell 76, 345-356.
    • (1994) Cell , vol.76 , pp. 345-356
    • Weis, K.1    Rambaud, S.2    Lavau, C.3    Jansen, J.4    Carvalho, T.5    Carmo-Fonseca, M.6    Lamond, A.7    Dejean, A.8
  • 66
    • 0033199695 scopus 로고    scopus 로고
    • Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body
    • Yeager, T. R., Neumann, A. A., Englezou, A., Huschtscha, L. I., Noble, J. R. and Reddel, R. R. (1999). Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body. Cancer Res. 59, 4175-4179.
    • (1999) Cancer Res , vol.59 , pp. 4175-4179
    • Yeager, T.R.1    Neumann, A.A.2    Englezou, A.3    Huschtscha, L.I.4    Noble, J.R.5    Reddel, R.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.